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Protein sorting upon exit from the endoplasmic reticulum.
Journal article

Protein sorting upon exit from the endoplasmic reticulum.

  • 2001-02-24
Published in:
  • Cell. - 2001
Adenosine Triphosphatases
Centrifugation, Density Gradient
Endoplasmic Reticulum
Fungal Proteins
Glycosylphosphatidylinositols
Golgi Apparatus
Immunologic Techniques
In Vitro Techniques
Kinetics
Membrane Glycoproteins
Protein Transport
Saccharomyces cerevisiae
Saccharomyces cerevisiae Proteins
Secretory Vesicles
Vesicular Transport Proteins
English It is currently thought that all secretory proteins travel together to the Golgi apparatus where they are sorted to different destinations. However, the specific requirements for transport of GPI-anchored proteins from the endoplasmic reticulum to the Golgi apparatus in yeast could be explained if protein sorting occurs earlier in the pathway. Using an in vitro assay that reconstitutes a single round of budding from the endoplasmic reticulum, we found that GPI-anchored proteins and other secretory proteins exit the endoplasmic reticulum in distinct vesicles. Therefore, GPI-anchored proteins are sorted from other proteins, in particular other plasma membrane proteins, at an early stage of the secretory pathway. These results have wide implications for the mechanism of protein exit from the endoplasmic reticulum.
Language
  • English
Open access status
closed
Identifiers
Persistent URL
https://fredi.hepvs.ch/global/documents/97405
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